ΠΡΡΠ΅ΠΊΡΠΈΠ²Π½Π°Ρ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΡ Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ Escherichia coli ΡΠ΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΡΡ Π³Π΅Π½ΠΎΠ² ΡΠΈΡΠΎΠΊΠΈΠ½ΠΎΠ² ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°: Π΄Π΅Π»Π΅ΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ Π²Π°ΡΠΈΠ°Π½ΡΠ° ΠΈΠ½ΡΠ΅ΡΠ»Π΅ΠΉΠΊΠΈΠ½Π°-4 (hil-4 ?2) ΠΈ Π½Π΅ΠΉΡΠΎΡΡΠΎΡΠΈΠ½Π° Π³Π»ΠΈΠ°Π»ΡΠ½ΠΎΠ³ΠΎ ΠΏΡΠΎΠΈΡΡ ΠΎΠΆΠ΄Π΅Π½ΠΈΡ (gdnf)
ΠΡΠΎΡΠ΅ΡΡ ΠΊΠΎ-ΡΡΠ°Π½ΡΠ»ΡΡΠΈΠΎΠ½Π½ΠΎΠ³ΠΎ ΡΠΎΡΠΌΠΈΡΠΎΠ²Π°Π½ΠΈΡ ΡΡΡΡΠΊΡΡΡΡ ΡΡΠΊΠ°ΡΠΈΠΎΡΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ Π±Π΅Π»ΠΊΠ° Π² Π±Π°ΠΊΡΠ΅ΡΠΈΠ°Π»ΡΠ½ΠΎΠΉ ΠΊΠ»Π΅ΡΠΊΠ΅ ΠΎΠ±Π»Π°Π΄Π°Π΅Ρ ΠΎΠ΄Π½ΠΎΠΉ Ρ Π°ΡΠ°ΠΊΡΠ΅ΡΠ½ΠΎΠΉ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΡΡ. ΠΡΠΈ ΡΡΠ°Π²Π½ΠΈΡΠ΅Π»ΡΠ½ΠΎ ΠΌΠ°Π»ΠΎΠΌ ΡΡΠΎΠ²Π½Π΅ ΠΏΡΠΎΠ΄ΡΠΊΡΠΈΠΈ Π³Π΅ΡΠ΅ΡΠΎΠ»ΠΎΠ³ΠΈΡΠ½ΠΎΠ³ΠΎ ΠΏΠΎΠ»ΠΈΠΏΠ΅ΠΏΡΠΈΠ΄Π° (0,01β0,1% ΠΎΡ ΡΡΠΌΠΌΠ°ΡΠ½ΠΎΠ³ΠΎ ΠΊΠ»Π΅ΡΠΎΡΠ½ΠΎΠ³ΠΎ Π±Π΅Π»ΠΊΠ°) ΡΠΎΠΎΡΠ²Π΅ΡΡΡΠ²ΡΡΡΠΈΠΉ Π±Π΅Π»ΠΎΠΊ, ΠΊΠ°ΠΊ ΠΏΡΠ°Π²ΠΈΠ»ΠΎ, ΡΠ°ΡΡΠ²ΠΎΡΠΈΠΌ, ΠΏΡΠΈ ΠΏΠΎΠ²ΡΡΠ΅Π½ΠΈΠΈ ΡΡΠΎΠ²Π½Ρ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠΈ ΠΎΠ±Π½Π°ΡΡΠΆΠΈΠ²Π°ΡΡΡΡ ΠΊΠ°ΠΊ ΡΠ°ΡΡΠ²ΠΎΡΠΈΠΌΡΠ΅, ΡΠ°ΠΊ ΠΈ Π½Π΅ΡΠ°ΡΡΠ²ΠΎΡΠΈΠΌΡΠ΅ ΡΠΎΡΠΌΡ Π±Π΅Π»ΠΊΠ°, Π° ΠΏΡΠΈ… Π§ΠΈΡΠ°ΡΡ Π΅ΡΡ >
Π‘ΠΏΠΈΡΠΎΠΊ Π»ΠΈΡΠ΅ΡΠ°ΡΡΡΡ
- Adams, J. Π. (1968) On the release of the formyl group from nascent protein. J. Mol. Biol. 33: 571−589.
- Adhya, S. and Gottesman, M. (1982) Promoter occlusion: transcription through a promoter may inhibit its activity. Cell 29: 939−944.
- Allen, S.P., Polazzi, J.O., Gierse, J.K., Easton, A.M. (1992) Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli. J. Bacteriol. 174:6936−6941.
- Arenas, E., Trupp, M., Akerud, P. & Ibanez, C.F. (1995) GDNF prevents degeneration and promotes the phenotype of brain noradrenergic neurons in vivo. Neuron 15:1465−1471.
- Atamas, S.P., Choy, J., Yurovsky, V.V., White, B. (1996) An alternative splice variant of human IL-4, IL-452, inhibits IL-4-stimulated T cell proliferation. J. Immunol. 156:435−441.
- Balakrishnan, R., Bolten, Π., Backman, K.C. (1994) A gene cassette for adapting Escherichia coli strains as hosts for a//-Int-mediated rearrangement and PL expression vectors. Gene 138: 101−104.
- Balbas, P., Bolivar, F. (1990) Design and construction of expression plasmid vectors in Escherichia coli. Methods Enzymol. 185: 14−37.
- Banchereau J., Bidaud, C., Fluckiger, A., Galibert, L., Garrone, P., Malisan, F. & Pandrau, D. (1993) Effects of interleukin 4 on human Π cell growth and differentiattion. Res. Immunol. 144:625−631.
- Baneyx, F. (1999) Recombinant protein expression in Escherichia coli. Current Opinion in Biotechnology. 10: 411−421.
- Bardwell, J. C. A. (1994) Building bridges: disulfide bond formation in the cell. Mol. Microbiol. 14: 199−205.
- Bechhofer, D. (1993) 59 mRNA stabilizers, p. 31−52. In J. G. Belasco and G. Brawerman (ed.), Control of messenger RNA stability. Academic Press, Inc., San Diego, Calif.
- Belasco, J. G., G. Nilsson, A. von Gabain, and S. N. Cohen. (1986) The stability of?. coli gene transcripts is dependent on determinants localized to specific mRNA segments. Cell 46:245−251.
- Ben-Bassat, A., Bauer, K., Chang, S.-Y., Myambo, K., Boosman, A., Chang, S. (1987) Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure. J. Bacteriol. 169: 751−757.
- Bessette, P-H., Aslund, F., Beckwith, J., Georgiou, G. (1999) Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sei. USA. 96:13 703−13 708.
- Bjornsson, A., S. Mottagui-Tabar, and L. A. Isaksson. (1996) Structure of the C-terminal end of the nascent peptide influences translation termination. EMBOJ. 15: 1696−1704.
- Blackwell, J. R. and Horgan, R. (1991) A novel strategy for production of a highly expressed recombinant protein in an active form. FEBS Lett. 295: 10— 12.
- Blight, M. A., Chervaux, C., and Holland, I. B. (1994) Protein secretion pathways in Escherichia coli. Curr. Opin. Biotechnol. 5: 468—474.
- Bogosian, G., Violand, B. N., Dorward-King, E. J., Workman, W. E., Jung, P. E., and Kane, J. F. (1989) Biosynthesis and incorporation into protein of norleucine by Escherichia coli. J. Biol. Chem. 264: 531−535.
- Bohn, M. (1999) A commentary on glial cell line-derived neurotrophic factor (GDNF). From a glial secreted molecule to gene therapy. Biochem Pharmacol. 57(2): 135−142.
- Bowden, G. A., and Georgiou, G. 1988. The effect of sugars on b-lactamase aggregation in Escherichia coli. Biotechnol. Prog. 4: 97−101.
- Bradford, M. M. (1976) A rapid and sensitive method of for the quantitation of microgram quantities of protein utilizing the priciple of protein-dye binding. Anal. Biochem. 72:248−254.
- Brinkmann, U., Mattes, R. E., and Buckel P. (1989) High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene 85: 109−114.
- Brosius, J., Erfle, M., Storella, J. Spacing of the -10 and -35 regions in the tac promoter. (1985) Effect on its in vivo activity. J Biol Chem. 260(6):3539−3544.
- Brosius, J., Ullrich A., Raker, M.A., Gray, A., Dull, T.J., Gutell, R.G., Noller, H.F. (1981) Construction and fine mapping of recombinant plasmids containing the rrnB ribosomal RNA operon of E.coli. Plasmid 6: 112−118.
- Brown, W.C. and Campbell, J.L. (1993) A new cloning vector and the expression strategy for genes encoding proteins toxic to Escherichia coli. Gene. 127: 99−103.
- Bukau, B., Horwich, A.L. (1998) The Hsp70 and Hsp60 chaperone machines. Cell 92: 351−366.
- Bukowski TP, Sedberry S, Richardson B. Straten. (2001) Is human chorionic gonadotropin useful for identifying and treating nonpalpable testis? J Urol. 165(l):221−226.
- Butler, J.S., Springer, M., Grunberg-Manago, M. (1987) AUU-to-AUG mutation in the initiator codon of the translation initiator factor IF3 abolishes translational autocontrol of its own gene (infC) in vivo. Proc. Natl. Acad. Sci. USA 84: 4022−4025.
- Carpousis, A.J., Vanzo, N.F., Raynal, L.C. (1999) mRNA degradation: a tail of poly (A) and multiprotein machines. Trends Genet. 15: 24−28.
- Chang, J.Y. and Swartz, J.R. (1993) Single-step solubilization and folding of IGF-I aggregates from Escherichia coli. In: Protein Folding in vivo and in vitro. Cleland J.I., Ed. ACS Symposium Series 526. Washington. D.C. p. 178 189.
- Chao, Y.-P., Chiang, C.-J., Lo T.-E., Fu, H. 2000. Overproduction of D-hydantoinase and carbamoylase in a soluble form in Escherichia coli. Appl. Microbiol Biotechnol. 54: 348−353.
- Cheah, K. C., Harrison, S., King, R., Crocker, L., Wells, J. R. E. and Robins, A. (1994) Secretion of eukaryotic growth hormones in Escherichia coli is influenced by the sequence of the mature proteins. Gene 138: 9−15.
- Chen, C.-Y. A., Beatty, J. T., Cohen, S. N., and Belasco, J. G. (1988) An intercistronic stem-loop structure functions as an mRNA decay terminator necessary but insufficient for puf mRNA stability. Cell 52: 609−619.
- Chen, G.-F. T., and Inouye, M. (1994). Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli. Genes Dev. 8: 2641−2652.
- Chen, G.-F. T., and Inouye, M. 1990. Suppression of the negative effect of minor arginine codons on gene expression: preferential usage of minor codons within the first 25 codons of the Escherichia coli genes. Nucleic Acids Res. 18: 1465−1473.
- Chen, H.-Y., Pomeroy-Cloney, L., Bjerknes, M., Tam, J., Jay, E. (1994) The influence of adenine-rich motifs in the 3' portion of the ribosome binding site on human IFN-y gene expression in Escherichia coli. J. Mol. Biol. 240: 2027.
- Chen, L.-H., S. A. Emory, A. L. Bricker, P. Bouvet, and J. G. Belasco. (1991) Structure and function of a bacterial mRNA stabilizer: Analysis of the 59 untranslated region of ompA mRNA. J. Bacteriol. 173: 4578−4586.
- Chen, W., Kallio, T., Bailey, J.E. (1995) Process characterization of a novel cross-regulation system for cloned protein production in Escherichia coli. Boitechnol. Prog. 11: 397−402.
- Chopin, M-C., Chopin, A., Ronault, A., Galleron, M. (1989) Insertion and amplification of foreign genes in the Lactococcus lactis subsp. lactis chromosome. Appl.Environ. Microbiol. 55:1769−1774.
- Clark, E. (1999) Protein refolding for industrial processes. Current Opinion in Biotechnology 12:202−207.
- Cleland, J. I., (1993) Impact of protein folding on biotechnology. In: Protein Folding in vivo and in vitro. Cleland J.I., Ed. ACS Symposium Series 526. Washington. D.C. p. 1−18.
- Coburb, G.A., Mackie, G.A. 1999. Degradation of mRNA in Escherichia coli: an old problem with some new twists. Prog. Nucleic Acid Res. Mol. Biol. 62: 55−108.
- Coyle, J.E., Jaeger, J., Gross, M., Robinson, C.V., Radford, S.E. (1997) Structural and mechanistic consequences of polypeptide binding by GroEL. Fold. Des. 2: 93−104.
- Crawford, R., Finbloom, D" Ohara, J., Paul W. & Meltzer, M. (1987) B cell stimulatory factor-1 (interleukin-4) activates macrophages for increased tumoricidal activity and expression of 1 a antigens. J. Immunol. 139:135−141.
- Dalboge, H., Dahl, H.-H. M., Pedersen, J., Hansen, J. W., Christensen, T. (1987) A novel enzymatic method for production of authentic hGH from an Escherichia coli produced hGH-precursor. Bio/Technology 5: 161−164.
- Derman, A. I., Prinz, W. A., Belin, D., and Beckwith, J. (1993). Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262: 1744−1747.
- Dix, D.B., and Thompson, R.C. (1989). Codon choice and gene expression: synonymous codons diffe in translation accuracy. Proc. Natl. Acad. Sci. USA 86: 6888−6893.
- Donovan, W. P., and S. R. Kushner. (1986) Polynucleotide phosphorylase and ribonuclease II are required for cell viability and mRNA turnover in Escherichia coli K-12. Proc. Natl. Acad. Sci. USA 83: 120−124.
- Duvoisin, R. M., D. Belin, and H. M. Krisch. (1986) A plasmid expression vector that permits stabilization of both mRNAs and proteins encoded by the cloned genes. Gene 45: 193−201.
- Emory, S. A., P. Bouvet, and J. G. Belasco. (1992) A 59-terminal stem-loop structure can stabilize mRNA in Escherichia coli. Genes Dev. 6: 135−148.
- Estrem, S.T., Gaal, T., Ross, W., Gourse, R. L. (1998) Identification of an UP element consensus sequence for bacterial promoters. Proc. Natl. Acad. Sci. USA. 95: 9761−9766.
- Etchegaray, J.P., Inouye, M. (1999) Translational enhancement by an element downstream of the initation codon in Escherichia coli. J. Biol. Chem. 274: 10 079−10 085.
- Fahnestock, S. R., Irwin, S. L., (1997)Synthetic spider dragline silk proteins and their production in Escherichia coli. Appl. Microbiol. Biotechnol. 47(l):23−32.
- Figge, J., Wright, C., Collins, C. J., Roberts, T. M., and Livingston, D. M. (1988) Stringent regulation of stably integrated chloramphenicol acetyl transferase genes by E. coli lac repressor in monkey cells. Cell 52:713−718.
- Fischer, B., Sumner, I., Goodenough, P., (1993) Isolation, renaturation, and formation of disulfide bonds of eukariotic proteins expressed in Escherichia coli as inclusion bodies. Biotechnol. Bioeng. 41: 3−13.
- Forrer, P. and Jaussi, R. (1998) High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda head protein D. Gene 224: 45−52.
- Frankel, S., Sohn R., Leinwand, L., (1991) The use of sarcosyl in generating soluble protein after bacterial expression. Proc. Natl. Acad. Sei. USA 88: 1192−1196.
- Friehs K, Reardon KF. (1993) Parameters influencing the productivity of recombinant E. coli cultivations. Adv. Biochem. Eng. Biotechnol. 48:53−58.
- Garcia, G. M., P. K. Mar, D. A. Mullin, J. R. Walker, and N. E. Prather. (1986) The E. coli dnaY gene encodes an arginine transfer RNA. Cell 45: 453−459.
- Georgiou, G. (1996) in Protein engineering: Principles and Practice (Cleland, J. L. and Craik, C. S., eds.), pp. 101−127, Wiley-Liss, New York.
- Georgiou, G., Valax, P. (1999) Isolation inclusion bodies from bacteria. Methods. Enzymol. 309:48−58.
- Giladi, H., Koby, S., Gottesman, M.E., Oppenheim, A.B. (1992) Supercoiling, integration host factor, and a dualpromoter system, participate in the control of the bacteriophage X pL promoter. J. Mol. Biol. 224: 937−948.
- Glare, E. M,. Divjak, M., Rolland, J.M., Walters, E.H. (1999) Asthmatic airway biopsy specimens are more likely to express the IL-4 alternative splice variant IL-4delta2. J Allergy Clin Immunol 104(5):978−982.
- Glascock, C.B., Weickert, M.J. (1998) Using chromosomal lacIQX to control expression of genes on high-copy number plasmids in Escherichia coli. Gene 223: 221−231.
- Goff, S. A. and Goldberg, A., L. (1985) Production of abnormal proteins in E. coli stimulates transcription of Ion and other heat shock genes. Cell 41:587 595.
- Gold, L. and Stormo, G.D. (1990) High-level translation initiation. Methods Enzymol. 185: 89−93.
- Goldman, E., Rosenberg, A. H., Zubay, G., and Studier, F. W. (1995) Consecutive low-usage leucine codons block translation only when near the 5'-end of a message in Escherichia coli. J. Mol. Biol. 245: 467−473.
- Gottesman, S. (1999) Regulation of proteolysis: developmental switches. Current Opinion in Microbiology 2:142−147.
- Grossman, T.H., Kawasaki, E.S., Punreddy, S.R., Osbune, M.S. (1998) Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability. Gene 209: 95−103.
- Gutman, G. A. and Hatfield, G. W. (1989) Nonrandom utilization of codon pairs in Escherichia coli. Proc. Natl. Acad. Sci. USA 86:3699−3703.
- Hall, M.N., Gabay, J., Debarbouille, M., Schwartz, M. (1982) A role for mRNA secondary structure in the control of translation initiation. Nature (London) 295:616−618.
- Hancock, R.E.W. (1983) Alternations in outer membrane permeability. Annu.Rev.Microbiol. 38: 237−247.
- Hayashi, M.N., Hayashi, M. (1985) Cloned DNA sequences that determine mRNA stability of bacteriophage
- Henderson, C.E., Philips, H.S., Pollock, R.A., Davies A.M., Armanini, M., Simmons, L., Moffet, B" Vandlen, R.A. & Simmons, L. (1994) GDNF: a potent survival factor for motoneurons present in peripheral nerve and muscle. Science 266:1062−1067.
- Higgins, C. F" H. C. Causton, G. S. C. Dance, and E. A. Mudd. (1993) The role of the 39 end in mRNA stability and decay, p. 13−30. In J. G. Belascoand G. Brawerman (ed.), Control of messenger RNA stability. Academic Press, Inc., San Diego, Calif.
- Hirota, Y., Suzuki, H., Nishimura, Y., Yasuda, S. 1977. On the process of cellular division in Escherichia coli: a mutant of E. coli lacking a murein-lipoprotein. Proc.Natl.Acad.Sci. USA 74: 1417−1422.
- Hottenrott, S., Schumann, T., Pluckthun, A., Fischer, G., Rahfeld, J.-U. (1997) The Escherichia coli SlyD is a metal ion-regulated peptidyl-prolyl cis/trans isomerase. J. Biol. Chem. 272: 15 697−15 701.
- Howard, M., Farrar, J., Hilfike, r M., Johnson, B., Takatsu, K., Hamaoka, T., Paul W. E. (1982) Identification of a T cell derived B cell growth factor distinct from interleukin-2. J. Exp. Med. 155:914−923.
- Hsiung, H. M., Cantrell, A., Luirink, J., Oudega, B., Veros, A. J., and Becker, G. W. (1989) Use of bacteriocin release protein in E. coli for excretion of human growth hormone into the culture medium. Bio/Technology 7: 267−271.
- Hsiung, H. M., Mayne, N. G., and Becker, G. W. (1986) High-level expression, efficient secretion and folding of human growth hormone in Escherichia coli. Bio/Technology 4: 991−995.
- Huh, K. R., Cho, E. H., Lee, S. O., Na, D. S. (1996) High level expression of human lipocortin (annexin) 1 in Escherichia coli. Biotechnol. Lett. 18: 163 168.
- Hwang, C., Sinskey, A. J., Lodish, H. F. (1992) Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496−1502.
- Illera, V., Perdandones, C., Stunz, L., Mower, D. & Ashman. (1993) Apoptosis in splenic B lymphocytes: regulation by protein kinase C and IL-4. J. Immunol. 151:3521−3526.
- Jaenicke, R., Rudolf, R. (1989) Folding protein, pp.191−223. In: T. E/ Creighton (ed.), Protein structure, a practical approach. Oxford University Press, Oxford, UK.
- Jonasson, P., Liljeqvist, S., Nygren, P-A., Stahl, S. (2002) Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli. Biotechnol. Appl. Biochem. 35:91−105.
- Kapust, R.B. and Waugh, D.S. (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sei. 8: 1668−1674.
- Kavanaugh, J. S., Rogers, P. H., Arnone, A. (1992) High-resolution X-ray study of deoxy recombinant human hemoglobins synthesized from b-glo-bins having mutated amino termini. Biochemistry 31: 8640−8647.
- Kenealy, W. R., Gray, J. E., Ivanoff, L. A., Tribe, D. E., Reed, D. L., Korant, B. D. and Petteway, S. R., Jr. (1987) Solubility of proteins overexpressed in Escherichia coli. Dev. Ind. Microbiol. 28: 45−52.
- Kern, I., and Ceglowski, P. (1995) Secretion of streptokinase fusion proteins from Escherichia coli cells through the hemolysin transporter. Gene 163: 53−57.
- Kimmenade, A., Bond, M. W., Schumacher, J. H., Laquoi, C., Kastelein, R. A. (1988) Expression, renaturation and purification of recombinant human interleukine 4 from Escherichia coli. Eur. J. Biochem. 173:109−114.
- Kitai, K., Kudo T., Nakamura, S., Masegi, T., Ichikawa, Y., and Horikoshi, K. 1988. Extracellular production of human immunoglobulin G Fe region (hlgG-Fc) by Escherichia coli. Appl. Microbiol. Biotechnol. 28: 52−56.
- Kleerebezem, M. and Tommassen, J. (1993) Expression of the pspA gene stimulates efficient protein export in Escherichia coli. Mol. Microbiol. 7: 947−956.
- Laemmli, V.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680−685.
- Lanzer, M., Bujard, H. (1988) Promoters largely determine the efficiency of repressor action. Proc. Natl. Acad. Sei. 85: 8973−8977.
- Lapchak, P.A., Gash, D. M., Jiao, S., Miller, P. J., Hilt, D. (1997) Glial cell line-derived neurotrophic factor: a novel therapeutic approach to treat motor dysfunction in Parkinson’s disease. Exp. Neurol. 144(1):29−34.
- Lee, Y., Oelkuct, M., Gentz, R. Method for pyrifying chemokines from inclusion bodies. US patent 1999 591 12 327.
- Liew, O.W., Choo A. B-H., Too, H.P. (1997) Parameters influencing the expression of mature glial-cell-line-derived neurotrophic factor in Escherichia coli. Biotechnol. Appl. Biochem. 25:223−233.
- Lin, L-F.H., Doherty, D.H., Lile, J.D., Bektesh, S & Collins, F. (1993) GDNF: a glial cell line-derived neurotrophic factor for midbrain dopaminergic neurons. Science 260:1130.
- Makrides, S.C. (1996) Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Reviews. 60:512−538.
- Minas, W., and Bailey, J. E. (1995) Co-overexpression ofprlF increases cell viability and enzyme yields in recombinant Escherichia coli expressing Bacillus stearothermophilus a-amylase. Biotechnol. Prog. 11: 403−411.
- Minsky, A., Summers, R. G., and Knowles, J. R. (1986) Secretion of beta-lactamase into the periplasm of Escherichia coli: evidence for a district release step associated with a conformational change. Proc. Natl. Acad. Sei. USA. 83:4180−4184.
- Miroux, B., Walker, J. (1996) Over-production of protein in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J.Mol.Biol. 260: 289−298.
- Mitchell, L., Davis, L. & Lipsky, P. (1989) Promotion of human T lymphocyte proliferation by IL-4. J. Immunol. 142:1548−1557.
- Muller, J., Oehler, S., Muller-Hill, B. (1996) Repression of lac promoter as a function of distance, phase and quality of an auxiliary lac operator. J. Mol. Biol. 257:21−29.
- O’Connor, C.D. and Timmis, K.N., (1987) Highly repressible expression system for cloning genes that specify potentially toxic proteins. J. Bacteriol. 169: 4457−4462.
- Olins, P. O., Rangwala, S. H. (1990) Vector for enhanced translation of foreign genes in Escherichia col. Methods Enzymol. 185: 115−119.
- Olins, P. O., Rangwala, S. H. (1989) A novel sequence element derived from bacteriophage T7 mRNA acts as an enhancer of translation of the lacZ gene in Escherichia coli. J. Biol. Chem. 264: 16 973−16 976.
- Olsen, M.K., Rockenbach, S.K., Curry, K.A., Tomich, C.-S.C. (1989) Enhancement of heterologous polypeptide expression by alterations in the ribosome-binding site sequence. J. Biotechnol. 9: 179−190.
- Olson, P., Zhang, Y., Olsen, D., Owens, A., Cohen, P., Nguyen, K., Ye, J-J., Bass, S., Mascarenhas, D.(1998) High-level expression of eukaryotic polypeptides from bacterial chromosomes. Protein. Expr. Purif. 14:160−166.
- Omer, C. A., Diehl, R. E., Krai, A. M. (1995) Bacterial expression and purification of human protein prenyltransferases using epitope-tagged, translationally coupled systems. Methods Enzymol 250: 3−12.
- Ozawa, K., Fan, D.S., Shen, Y., Muramatsu, S., Fujimoto, K., Ikeguchi, K., Ogawa, M., Urabe, M., Kume, A., Nakano, I. (2000) Gene therapy of Parkinson’s disease using adeno-associated virus (AAV) vectors. J. Neural. Transm. Suppl. 58:181 -191.
- Pe’rez-Pe'rez, J., G. Ma’rquez, J.-L. Barbero, and J. Gutie’rrez. (1994) Increasing the efficiency of protein export in Escherichia coft. Bio/Technology 12: 178−180.
- Peredelchuk, M. Y., Bennett, G. N. (1997) A method for construction of E. coli strains with multiple DNA insertions in the chromosome. Gene 187:231 238.
- Phadtare, S., Alsina, J., Inouye, M. (1999) Cold-shock response and cold-shock proteins. Curr. Opin. Microbiol. 2: 175−180.
- Poole, E. S., Brown, C. M., and Tate, W. P. (1995) The identity of the base following the stop codon determines the efficiency of in vivo translational termination in Escherichia coli. EMBOJ. 14: 151−158.
- Proba, K., Ge L. M., Pluckthun, A. (1995) Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: influence of thioredoxin reductase (TrxB). Gene 159: 203−207.
- Pryor, K.D. and Leiting, B. 1997. High level expression of soluble proteins in Escherichia coli using a His6-tag and maltose-binding protein double-affinity fusion system. Protein Expr. Purif10: 309−319.
- Przybycien, T.M., Dunn, J.P., Valax, P., Georgiou, G. (1994)Secondary structure characterization of p-lactamase inclusion bodies. Protein Eng. 7:131−137.
- Pugsley, A. P. and Schwartz, M. (1985) Export and secretion of proteins by bacteria. FEMS Microbiol. Rev. 32: 3−38.
- Ramer, M.S., Priestly, J.V. & McMahon, S. B. (2000) Functional regeneration of sensory axons into the adult spinal cord. Nature 403:312−316.
- Richardson, J.P. and Greenblatt, J. (1996) Control of RNA chain elongation and termination, p. 822−848. In F.C. Neidhardt, R. Curtiss III, J.L. Ingraham, E.C.C. Lin K.B.Low, B. Magasanik, W.S. Reznikoff, M. Riley M. Schaechter and H.E. Umbarger.
- Ringquist, S., Shinedling, S., Barrick, D., Green L., Binkley, J., Stormo, G.D., Gold, L. (1992) Translation initiation in Escherichia coli: sequence within the ribosome-binding site. Mol.Microbiol. 6: 1219−1229.
- Rudiger, S., Germeroth, L., Schneider-Mergener, J., Bukau, B. (1997) Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16: 1501−1507.
- Russell, D., R., Bennett, G. N. (1982) Construction and analysis of in vivo activity of E. coli promoter hybrids and promoter mutants that alter the -35 to -10 spacing. Gene 20(2):231−243.
- Sachdev, D. and Chirgwin, J.M. (1998) Order of fusions between bacterial and mammalian proteins can determine solubility in Escherichia coli. Biochem. Biophys. Res. Commun. 244: 933−937.
- Sagava, H., Ohshima, A., Kato I. (1996) A tightly regulated expression system in Escherichia coli with SP6 RNA polymerase. Gene 168: 37−41.
- Sambrook, J., Fritsch E., Maniatis T.// Molecular cloning. A Laboratory Manual. New York: Cold Spring Harbor, 1989.
- Sandman, K., Grayling, R. A., Reeve, J. N. (1995). Improved N-terminal processing of recombinant proteins synthesized in Escherichia coli. Bio/Technology 13: 504−506.
- Sanger, F., Nicklen, S., Coulson, A. R. (1977) DNA sequencing with chain-terminating inhibitors. Proc. Natl Acad. Sci. USA 74:5463−5467.
- Schatz, G. and Dobberstein, B. (1996) Common principles of protein translocation across membranes. Science 271: 1519−1526.
- Schauder, B., McCarthy, J. E. G. (1989) The role of bases upstream of the Shine-Dalgarno region and in the coding sequence in the control of geneexpression in Escherichia coli: translation and stability of mRNAs in vivo. Gene 78: 279−283.
- Schein, C. H. (1991) Optimizing protein folding to the native state in bacteria. Curr. Opin. Biotechnol. 2:746.
- Schein, C. H. (1993) Solubility and secretability. Curr. Opin. Biotechnol. 4: 456—461.
- Schumperli, D., McKenney, K., Sobieski, D.A., Rosenberg, M. (1982) Translation coupling an intercistronic boundary of the Escherichia coli galactose operon. Cell 30: 865−871.
- Scolnik, E., R. Tompkins, T. Caskey, and M. Nirenberg. (1968) Release factors differing in specificity for terminator codons. Proc. Natl. Acad. Sei. USA 61:768−774.
- Sharp, P. M., and Bulmer, M. (1988) Selective differences among translation termination codons. Gene 63:141−145.
- Shine, J., and L. Dalgarno (1974) The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: complementarity to nonsense triplets and ribosome binding sites. Proc. Natl. Acad. Sei. USA 71: 1342−1346.
- Siegele, D.A. and Hu, J.C. (1997) Gene expression from plasmids containing the araBAD promoter at subsaturating inducer concentrations represents mixed populations. Proc. Natl. Acad. Sei. USA. 94: 8168−8172.
- Skerra, A. (1993) Bacterial expression of immunoglobulin fragments. Curr. Opin. Immunol. 5: 256−262.
- Snyder, W. B. and Silhavy, T. J. (1992) Enhanced export of b-galactosidase fusion proteins in prlF mutants is Lon dependent. J. Bacteriol. 174:5661−5668.
- Sorg, R.V., Enczmann, J., Sorg, U.R., Schneider E. M, Wernet, P. (1993) Identification of an alternatively spliced transcript of human interleukin-4 lacking the sequence encoded by exon 2. Exp. Hematol. 21:560−563.
- Sprengart, M. L., Fuchs, E., Porter, A. G. (1996) The downstream box: an efficient and independent translation initiation signal in Escherichia coli. EMBOJ. 15: 665−674.
- Stanssens P., Remaut E., Fiers W. (1985) Alterations upstream from the Shine-Dalgarno region and their effect on bacteral gene expression. Gene 36: 211−223.
- Sugimoto, S., Yokoo, Y., Hatakeyama, N., Yotsuj, A., Teshiba, S., and Hagino, H. (1991) Higher culture pH is preferable for inclusion body formation of recombinant salmon growth hormone in Escherichia coli. Biotechnol. Lett. 13: 385−388.
- Summers, D. (1998) Timing, self-control and a sense of direction are the secrets of multicopy plasmid stability. Mol. Microbiol. 29:1137−1145.
- Swartz, R. (2001) Advances in Escherichia coli production of therapeutic proteins. Curr. Opin. Biotechnol 12:195−201.
- Tagawa A, Kashima R, Kaneda K, Nakayama M, Ono S, Shimizu N. (2000) Polymyositis successfully treated with surgical resection of colon cancer. Eur Neurol. 44(4):251−252.
- Tate, W. P., and C. M. Brown. (1992) Translational termination: «stop» for protein synthesis or «pause» for regulation of gene expression. Biochemistry 31: 2443−2450.
- Tessier, L.-H., Sondermeyer, P., Faure T., Dreyer, D., Benavente, A., Villeval, D., Courtney, M., Lecocq, J.-P. (1984) The influence of mRNA primary and seconary structure on human IFN-y gene expression in E.coli. Nucleic Acids Res. 12: 7663−7675.
- Thomas, C.D., Modha, J., Razzaq, T.M., Cullis, P.M., Rivett, A.J. (1993) Controlled high-level expression of the Ion gene of Escherichia coli allows overproduction of Lon protease. Gene 136: 237−242.
- Thomas, J.G., Ayling, A., Baneyx, F. (1997) Molecular chaperones, folding catalysis and the recovery of active recombinant proteins from E. coli: to fold or to refold. Appl. Biochem. Biotechnol. 66: 197−238.
- Tocatlidis, K., Dhurjati, P., Millet, J., Beguin, P., Aubert, J.-P. (1991) High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D. FEBSLett. 282:205−209.
- Tolentino, G.J., Meng, S.-Y., Bennet, G.N., San, K.-Y. (1992) A pH-regulated promoter for the expression of recombinant proteins in Escherichia coli. Biotechnol. Letters. 14: 157−162.
- Tsung, K., Inouye, S., Inouye, M. (1989) Factors affecting the efficiency of protein synthesis in Escherichia coli. Production of a polypeptige of more than 6000 amino acid residues. J. Biol. Chem. 264: 4428−4433.
- TzarevaN. V., Makhno V. I., Boni I. V. (1994) Ribosome-messenger recognition in the absence of the Shine-Dalgarno interactions. FEBS Lett. 337: 189−194.
- Varshavsky, A. (1996) The N-end rule: Functions, mysteries, uses. Proc.Natl.Acad.Sci. USA 93: 12 142−12 149.
- Vasina, J. A., Peterson, M. S., Baneyx, F. (1998) Scale-up and optimization of the low-temperature inducible cspA promoter system. Biotechnol. Prog. 14:714−721.
- Voskuil, M.I. and Chambliss, G.N. (1998) The -16 region of Bacillus subtilis and other gram-positive bacterial promoters. Nucl. Acids Res. 26: 3584−3590.
- Warne, S.R., Thomas, C.M., Nugent, M.E., Tacon, W.C.A. (1986) Use of modified Escherichia coli trpR gene to obtain tight regulation of high-copy number expression vectors. Gene 46: 103−112.
- Wier, U., Sparks, J. (1987) Purification and renaturation of recombinant human interleukine-2. Biochem. J. 245:85−91.
- Wilhelm, O. G., Jaskunas, S. R., Vlahos, C. J., Bang, N. U. (1990) Functional properties of the recombinant kringle-2 domain of tissueplasminogen activator produced in Escherichia coli. J. Biol. Chem. 265:14 606−14 611.
- Wilkinson, D. L. and Harrison, R. G. (1991) Predicting the solubility of recombinant proteins in Escherichia coli. Bio/Technology 9: 443−448.
- Williams, S. G., Cranenburgh, R. M., Weiss, A-M. E., Wrighton, C. J., Sheratt, D. J., Hanak, J. J. (1998) Repressor tiyration: a novel system for selection and stable maintenance of recombinant plasmids. Nucleic Acids Res. 26:2120−2124.
- Wong, H. C., and S. Chang. March (1990) 39-Expression enhancing fragments and method. U.S. patent 4,910,141.
- Yabuta, M., Onai-Miura, S., Ohsuye, K. (1995) Thermo-inducible expression of a recombinant fusion protein by Escherichia coli lac repressor mutants. J. Biotechnol. 39: 67−73.
- Yamamoto, T., and F. Imamoto. (1975) Differential stability of trp messenger RNA synthesized originating at the trp promoter and pL promoter of lambda trp phage. J. Mol. Biol. 92: 289−309.
- Yasueda, H., Nagase, K., Hosoda, A., Akiyama, Y., Yamada, K. (1990) High-level direct expression of semi-synthetic human interleukine-6 in Escherichia coli. And production of N-terminus Met-free product. Bio/Technol. 8:1036−1040.
- Yasukawa, T., Kaneiishii, C., Maekawa, T., Fujimoto, J., Yamamoto, T. And Ishii, S. (1995) Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. J. Biol. Chem. 270: 2 532 825 331.
- Zav’yalov, V.P., Denesyuk, A. I., White, B., Yurovsky, V. V., Atamas, S. P., Korpela, T. (1997) Immunol. Lett. 58:149−152.
- Zhang, S., G. Zubay, and E. Goldman. (1991) Low usage codons in Escherichia coli, yeast, fruit fly and primates. Gene 105: 61−72.
- Zhang, Y., Olsen, D.R., Nguyen, K.B., Olson, P. S., Rhodes, E.T., Mascarenhas, D. (1998) Expression of eukaryotic proteins in soluble form in Escherichia coli. Protein Expr. Purif. 12: 159−165.
- Zum, A.D., Widmer, H.R., Aebischer, P. (2001) Sustained delivery of GDNF: towards a treatment for Parkinson’s disease. Brain Res. Rev. 36:222 229.
- ΠΠ»ΡΡΠΌΠ°Π½ Π.Π., ΠΡΠΈΡΡΠ½ JI.P., Π‘ΠΌΠΈΡΠ½ΠΎΠ² C.B., ΠΠ°Π»ΡΠΆΡΠΊΠΈΠΉ B.E., ΠΠ°ΡΠΊΠΎ C.B. (1997) Π‘ΠΎΠ·Π΄Π°Π½ΠΈΠ΅ ΡΡΠ°ΠΌΠΌΠ°-ΠΏΡΠΎΠ΄ΡΡΠ΅Π½ΡΠ° ΡΠ΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΠΎΠ³ΠΎ Ρ-ΠΈΠ½ΡΠ΅ΡΡΠ΅ΡΠΎΠ½Π° Π±ΡΠΊΠ°, ΠΏΡΠΈΠ³ΠΎΠ΄Π½ΠΎΠ³ΠΎ Π΄Π»Ρ ΡΡΡΠ΅ΠΊΡΠΈΠ²Π½ΠΎΠ³ΠΎ Π±ΠΈΠΎΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΎΠ³ΠΎ ΠΏΡΠΎΠΈΠ·Π²ΠΎΠ΄ΡΡΠ²Π°. ΠΠΈΠΎΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΡ № 11−12, Π‘. 3−13.
- ΠΠ΅Π±Π°Π±ΠΎΠ² Π. Π., ΠΠ΄Π°Π½ΠΎΠ²Π° Π. Π. Π Π΄Ρ. Π¨ΡΠ°ΠΌΠΌΡ Π. coli ΠΠΠΠΠΠ΅Π½Π΅ΡΠΈΠΊΠ° VL 334(pYN7) ΠΈ ΠΠΠΠΠΠ΅Π½Π΅ΡΠΈΠΊΠ° VL. 334(pYN6) ΠΏΡΠΎΠ΄ΡΡΠ΅Π½ΡΡ L -ΡΡΠ΅ΠΎΠ½ΠΈΠ½Π° ΠΈ ΡΠΏΠΎΡΠΎΠ± ΠΈΡ ΠΏΠΎΠ»ΡΡΠ΅Π½ΠΈΡ: ΠΠ°ΡΠ²ΠΊΠ° № 4 191 345/13 Π‘Π‘Π‘Π . 1979.
- ΠΠ³ΠΎΡΠΎΠ²Π° Π.Π., Π‘ΠΌΠΈΡΠ½ΠΎΠ² Π. Π. (1999) ΠΠΎΠ²ΡΠ΅ Π²ΠΎΠ·ΠΌΠΎΠΆΠ½ΠΎΡΡΠΈ ΠΈΠΌΠΌΡΠ½ΠΎΡΠ΅ΡΠ°ΠΏΠΈΠΈ Ρ ΠΈΡΠΏΠΎΠ»ΡΠ·ΠΎΠ²Π°Π½ΠΈΠ΅ΠΌ Π ΠΎΠ½ΠΊΠΎΠ»Π΅ΠΉΠΊΠΈΠ½Π° Π² ΡΠ΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΠΎΠ³ΠΎ ΠΈΠ½ΡΠ΅ΡΠ»Π΅ΠΉΠΊΠΈΠ½Π°-2 ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°. Terra Medica, 2:15.
- ΠΡΠ»Π°Π³ΠΈΠ½Π° M. Π., Π‘ΠΊΠ°ΠΏΡΠΎΠ²Π° Π. Π., ΠΠ°ΡΡΠΈΠΊΠΎΠ²Π° Π. Π., ΠΡΡΠΊΠΈΠ½ Π. Π., ΠΠΆΠ°Π΅Π² Π. Π. (1990) Π-ΡΠΎΡΡΠ°ΡΠ½ΡΠΉ ΠΌΠ΅ΡΠΎΠ΄ Π² ΡΠΈΠ½ΡΠ΅Π·Π΅ ΡΡΡΡΠΊΡΡΡΠ½ΠΎΠ³ΠΎ Π³Π΅Π½Π° ΠΈΠ½ΡΠ΅ΡΠ»Π΅ΠΉΠΊΠΈΠ½Π°-4 ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°. ΠΠΈΠΎΠΎΡΠ³Π°Π½ΠΈΡΠ΅ΡΠΊΠ°Ρ Ρ ΠΈΠΌΠΈΡ 16(5):625−629.
- ΠΠ°ΡΠΊΠΎ C.B., 1998. ΠΠΏΡΠΈΠΌΠΈΠ·Π°ΡΠΈΡ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠΈ ΡΡΠΆΠ΅ΡΠΎΠ΄Π½ΡΡ Π³Π΅Π½ΠΎΠ² Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ E.coli. ΠΠΈΠΎΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΡ 6:3−23.
- ΠΡΠΈΡΡΠ½ Π.Π ., ΠΠ»ΡΡΠΌΠ°Π½ Π. Π. (1995) Π Π΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΡΠ΅ ΡΡΠ°ΠΌΠΌΡ Escherichia coli, ΠΎΠ±Π΅ΡΠΏΠ΅ΡΠΈΠ²Π°ΡΡΠΈΠ΅ Π²ΡΡΠΎΠΊΠΈΠΉ ΡΡΠΎΠ²Π΅Π½Ρ ΡΠΊΡΠΏΡΠ΅ΡΡΠΈΠΈ ΠΈΠ½ΡΠ΅ΡΠ»Π΅ΠΉΠΊΠΈΠ½Π°-3 ΠΈ ΠΈΠ½ΡΠ΅ΡΠ»Π΅ΠΉΠΊΠΈΠ½Π°-4 ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°. ΠΠΎΠ²ΡΠ΅ ΠΌΠ΅Π΄ΠΈΡΠΈΠ½ΡΠΊΠΈΠ΅ ΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΠΈ 59(1):83−85.
- ΠΡΠΈΡΡΠ½ Π.Π ., Π‘ΠΌΠΈΡΠ½ΠΎΠ² C.B., ΠΠ»ΡΡΠΌΠ°Π½ Π. Π., Π‘Π°ΠΌΡΠΎΠ½ΠΎΠ²Π° H.H., Π₯ΠΎΠ΄ΡΠΊΠΎΠ²Π° A.B., ΠΠ°ΡΠΈΠ»Π΅Π½ΠΊΠΎ Π . Π. (1999) ΠΡΠΎΠ΄ΡΠΊΡΠΈΡ ΡΠ΅ΠΊΠΎΠΌΠ±ΠΈΠ½Π°Π½ΡΠ½ΠΎΠ³ΠΎ hIL-452 -ΠΏΡΠΈΡΠΎΠ΄Π½ΠΎΠΉ ΠΈΠ·ΠΎΡΠΎΡΠΌΡ ΠΈΠ½ΡΠ΅ΡΠ»Π΅ΠΉΠΊΠΈΠ½Π°-4 ΡΠ΅Π»ΠΎΠ²Π΅ΠΊΠ°, Π² ΠΊΠ»Π΅ΡΠΊΠ°Ρ Escherichia coli. ΠΠΈΠΎΠΎΡΠ³Π°Π½ΠΈΡΠ΅ΡΠΊΠ°Ρ Ρ ΠΈΠΌΠΈΡ 25(8):623−628.
- Π‘ΡΡΠΎΠ½Π³ΠΈΠ½ Π. Π―. (1990) ΠΠΎΠ»Π΅ΠΊΡΠ»ΡΡΠ½ΠΎ-Π±ΠΈΠΎΠ»ΠΎΠ³ΠΈΡΠ΅ΡΠΊΠΈΠ΅ ΠΎΡΠ½ΠΎΠ²Ρ ΡΡΡΡΠΊΡΡΡΠ½ΠΎ-ΡΡΠ½ΠΊΡΠΈΠΎΠ½Π°Π»ΡΠ½ΡΡ ΠΎΡΠΎΠ±Π΅Π½Π½ΠΎΡΡΠ΅ΠΉ Π±Π΅Π»ΠΊΠΎΠ² — ΠΏΡΠΎΠ΄ΡΠΊΡΠΎΠ² Π³Π΅ΡΠ΅Ρ ΠΎΠ»ΠΎΡΠΈΡΠ½ΠΎΠ³ΠΎ ΠΌΠΈΠΊΡΠΎΠ±Π½ΠΎΠ³ΠΎ ΡΠΈΠ½ΡΠ΅Π·Π°.// ΠΠ΅Π½Π΅ΡΠΈΠΊΠ° ΠΏΡΠΎΠΌΡΡΠ»Π΅Π½Π½ΡΡ ΠΌΠΈΠΊΡΠΎΠΎΡΠ³Π°Π½ΠΈΠ·ΠΌΠΎΠ² ΠΈ Π±ΠΈΠΎΡΠ΅Ρ Π½ΠΎΠ»ΠΎΠ³ΠΈΡ. ΠΠΎΡΠΊΠ²Π°, ΠΠ°ΡΠΊΠ°, Ρ. 240.